Cationic amino acid transport by two renal epithelial cell lines: LLC-PK1and MDCK cells

1985 ◽  
Vol 123 (1) ◽  
pp. 144-150 ◽  
Author(s):  
Francisco V. Sepúlveda ◽  
Jeremy D. Pearson
1993 ◽  
Vol 265 (1) ◽  
pp. F137-F145 ◽  
Author(s):  
D. P. Jones ◽  
L. A. Miller ◽  
R. W. Chesney

We characterized taurine transport in two continuous renal epithelial cell lines: LLC-PK1, derived from the proximal tubule of the pig, and the Madin-Darby canine kidney (MDCK), which was originated from the distal tubule of the dog. In the LLC-PK1 cell line, taurine transport is greatest at the apical surface of the cell, whereas in the MDCK cell line taurine transport is greatest at the basolateral surface. Both apical and basolateral surfaces of LLC-PK1 and MDCK cells exhibit an adaptive response to the extracellular taurine concentration (medium taurine concentration). Only the basolateral surface of the MDCK cell responded to hyperosmolality with increased taurine accumulation. This indicates differential control of the beta-amino acid transport system by substrate and external tonicity. The function of the beta-amino acid transport system may be different depending on the cell. In the LLC-PK1 cell, there is net transepithelial movement of taurine and changes in transporter activity in response to supply of substrate. In contrast, taurine accumulation by the MDCK cell appears to be a mechanism for adaptation to osmotic stress.


1984 ◽  
Vol 66 (1) ◽  
pp. 81-93
Author(s):  
F.V. Sepulveda ◽  
J.D. Pearson

We have studied the cell-to-cell passage of uridine nucleotides in two renal epithelial cell lines (LLC-PK1 and MDCK) and in porcine aortic endothelial cells (PAE). All three cell types incorporated tritiated uridine. After a 3 h incubation the radioactivity was predominantly in the form of acid-soluble compounds, mainly UTP. Prelabelled LLC-PK1 or MDCK cells were unable to transfer radioactivity to added adjacent, non-labelled cells, whereas PAE cells readily formed communicating intercellular junctions, as judged by autoradiographic analysis after a 3 h co-culture period. Cell-to-cell communication in either of the renal cell lines was not promoted by treatment with dibutyryl cyclic AMP and methylisobutylxanthine. Radioactivity incorporated into the acid-insoluble pool was not available for intercellular transfer, as assessed in experiments in which cells were prelabelled 24 h before co-culture.


1998 ◽  
Vol 273 (24) ◽  
pp. 14663-14666 ◽  
Author(s):  
Benjamin Nicholson ◽  
Tatsuya Sawamura ◽  
Tomoh Masaki ◽  
Carol L. MacLeod

2005 ◽  
Vol 288 (2) ◽  
pp. C290-C303 ◽  
Author(s):  
Tiziano Verri ◽  
Cinzia Dimitri ◽  
Sonia Treglia ◽  
Fabio Storelli ◽  
Stefania De Micheli ◽  
...  

Information regarding cationic amino acid transport systems in thyroid is limited to Northern blot detection of y+LAT1 mRNA in the mouse. This study investigated cationic amino acid transport in PC cell line clone 3 (PC Cl3 cells), a thyroid follicular cell line derived from a normal Fisher rat retaining many features of normal differentiated follicular thyroid cells. We provide evidence that in PC Cl3 cells plasmalemmal transport of cationic amino acids is Na+ independent and occurs, besides diffusion, with the contribution of high-affinity, carrier-mediated processes. Carrier-mediated transport is via y+, y+L, and b0,+ systems, as assessed by l-arginine uptake and kinetics, inhibition of l-arginine transport by N-ethylmaleimide and neutral amino acids, and l-cystine transport studies. y+L and y+ systems account for the highest transport rate (with y+L > y+) and b0,+ for a residual fraction of the transport. Uptake data correlate to expression of the genes encoding for CAT-1, CAT-2B, 4F2hc, y+LAT1, y+LAT2, rBAT, and b0,+AT, an expression profile that is also shown by the rat thyroid gland. In PC Cl3 cells cationic amino acid uptake is under TSH and/or cAMP control (with transport increasing with increasing TSH concentration), and upregulation of CAT-1, CAT-2B, 4F2hc/y+LAT1, and rBAT/b0,+AT occurs at the mRNA level under TSH stimulation. Our results provide the first description of an expression pattern of cationic amino acid transport systems in thyroid cells. Furthermore, we provide evidence that extracellular l-arginine is a crucial requirement for normal PC Cl3 cell growth and that long-term l-arginine deprivation negatively influences CAT-2B expression, as it correlates to reduction of CAT-2B mRNA levels.


1989 ◽  
Vol 1010 (3) ◽  
pp. 311-317 ◽  
Author(s):  
Christoph Korbmacher ◽  
Wolfgang Schulz ◽  
Michael König ◽  
Harald Siebe ◽  
Ingrid Lichtenstein ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document